ACAD8_BOVIN
ID ACAD8_BOVIN Reviewed; 416 AA.
AC Q0NXR6; A1A4N5;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Isobutyryl-CoA dehydrogenase, mitochondrial;
DE EC=1.3.8.- {ECO:0000250|UniProtKB:Q9UKU7};
DE AltName: Full=Acyl-CoA dehydrogenase family member 8;
DE Short=ACAD-8;
DE Flags: Precursor;
GN Name=ACAD8;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX PubMed=17498629; DOI=10.1016/s1673-8527(07)60033-2;
RA Li H., Xu S., Gao X., Ren H.;
RT "Structure of the bovine ACAD8 gene and the association of its polymorphism
RT with the production traits.";
RL J. Genet. Genomics 34:315-320(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal muscle;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Isobutyryl-CoA dehydrogenase which catalyzes one of the steps
CC of the valine catabolic pathway. To a lesser extent, is also able to
CC catalyze the oxidation of (2S)-2-methylbutanoyl-CoA.
CC {ECO:0000250|UniProtKB:Q9UKU7}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-methylpropanoyl-CoA + H(+) + oxidized [electron-transfer
CC flavoprotein] = (2E)-2-methylpropenoyl-CoA + reduced [electron-
CC transfer flavoprotein]; Xref=Rhea:RHEA:44180, Rhea:RHEA-COMP:10685,
CC Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57338,
CC ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:62500;
CC Evidence={ECO:0000250|UniProtKB:Q9UKU7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44181;
CC Evidence={ECO:0000250|UniProtKB:Q9UKU7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2S)-2-methylbutanoyl-CoA + H(+) + oxidized [electron-transfer
CC flavoprotein] = (2E)-2-methylbut-2-enoyl-CoA + reduced [electron-
CC transfer flavoprotein]; Xref=Rhea:RHEA:48256, Rhea:RHEA-COMP:10685,
CC Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57337,
CC ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:88166;
CC Evidence={ECO:0000250|UniProtKB:Q9UKU7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48257;
CC Evidence={ECO:0000250|UniProtKB:Q9UKU7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + oxidized [electron-transfer flavoprotein] + propanoyl-
CC CoA = acryloyl-CoA + reduced [electron-transfer flavoprotein];
CC Xref=Rhea:RHEA:31287, Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57367, ChEBI:CHEBI:57392,
CC ChEBI:CHEBI:57692, ChEBI:CHEBI:58307;
CC Evidence={ECO:0000250|UniProtKB:Q9UKU7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31288;
CC Evidence={ECO:0000250|UniProtKB:Q9UKU7};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:Q9UKU7};
CC -!- PATHWAY: Amino-acid degradation; L-valine degradation.
CC {ECO:0000250|UniProtKB:Q9UKU7}.
CC -!- SUBUNIT: Homotetramer, formed by a dimer of dimers.
CC {ECO:0000250|UniProtKB:Q9UKU7}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q9UKU7}.
CC -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DQ435444; ABD97096.1; -; mRNA.
DR EMBL; DQ435445; ABD97097.1; -; Genomic_DNA.
DR EMBL; BC126750; AAI26751.1; -; mRNA.
DR RefSeq; NP_001069019.1; NM_001075551.1.
DR AlphaFoldDB; Q0NXR6; -.
DR SMR; Q0NXR6; -.
DR STRING; 9913.ENSBTAP00000017188; -.
DR PaxDb; Q0NXR6; -.
DR PeptideAtlas; Q0NXR6; -.
DR Ensembl; ENSBTAT00000017188; ENSBTAP00000017188; ENSBTAG00000012937.
DR GeneID; 512070; -.
DR KEGG; bta:512070; -.
DR CTD; 27034; -.
DR VEuPathDB; HostDB:ENSBTAG00000012937; -.
DR VGNC; VGNC:25522; ACAD8.
DR eggNOG; KOG0140; Eukaryota.
DR GeneTree; ENSGT00940000157590; -.
DR InParanoid; Q0NXR6; -.
DR OMA; NMATWML; -.
DR OrthoDB; 819314at2759; -.
DR UniPathway; UPA00362; -.
DR Proteomes; UP000009136; Chromosome 15.
DR Bgee; ENSBTAG00000012937; Expressed in caput epididymis and 104 other tissues.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IEA:InterPro.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR GO; GO:0006574; P:valine catabolic process; IEA:UniProtKB-UniPathway.
DR CDD; cd01162; IBD; 1.
DR Gene3D; 1.10.540.10; -; 1.
DR Gene3D; 2.40.110.10; -; 1.
DR InterPro; IPR006089; Acyl-CoA_DH_CS.
DR InterPro; IPR006091; Acyl-CoA_Oxase/DH_mid-dom.
DR InterPro; IPR046373; Acyl-CoA_Oxase/DH_mid-dom_sf.
DR InterPro; IPR036250; AcylCo_DH-like_C.
DR InterPro; IPR009075; AcylCo_DH/oxidase_C.
DR InterPro; IPR013786; AcylCoA_DH/ox_N.
DR InterPro; IPR037069; AcylCoA_DH/ox_N_sf.
DR InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom.
DR InterPro; IPR034178; IBD.
DR Pfam; PF00441; Acyl-CoA_dh_1; 1.
DR Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR Pfam; PF02771; Acyl-CoA_dh_N; 1.
DR SUPFAM; SSF47203; SSF47203; 1.
DR SUPFAM; SSF56645; SSF56645; 1.
DR PROSITE; PS00072; ACYL_COA_DH_1; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Branched-chain amino acid catabolism; FAD; Flavoprotein;
KW Mitochondrion; Oxidoreductase; Reference proteome; Transit peptide.
FT TRANSIT 1..23
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 24..416
FT /note="Isobutyryl-CoA dehydrogenase, mitochondrial"
FT /id="PRO_0000253024"
FT ACT_SITE 399
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9UKU7"
FT BINDING 159..168
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:Q9UKU7"
FT BINDING 168
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9UKU7"
FT BINDING 192..194
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:Q9UKU7"
FT BINDING 275..278
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9UKU7"
FT BINDING 303
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250|UniProtKB:Q9UKU7"
FT BINDING 313..314
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250|UniProtKB:Q9UKU7"
FT BINDING 372..376
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250|UniProtKB:Q9UKU7"
FT BINDING 401..403
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:Q9UKU7"
FT BINDING 411
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9UKU7"
FT MOD_RES 51
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9D7B6"
FT MOD_RES 51
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9D7B6"
FT MOD_RES 232
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9D7B6"
FT MOD_RES 272
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9D7B6"
SQ SEQUENCE 416 AA; 45307 MW; 86BE48848C2C92DC CRC64;
MMLRGGCQRV GARLRGLRRG PRGPADGARR GVVSCIDPSM GLSEEQKEFQ KVAFNFAARE
MAPHMAEWDQ KELFPVDTMR KAAQLGFGGV YVQTDVGGAG LSRLDTSIIF EALATGCTST
TAYMSIHNMC VWIIDRFGSE EQRHRLCPPL CTMEKFASYC LTEPGSGSDA ASLMTSAVRQ
HDHYILNGSK AFISGGGEAD IYVVMCRTGG PGPRGISCVV VEKGTPGLSF GKKEKKVGWN
SQPTQAVIFE DCAVPVANRI GDEGQGFLIA MKGLNGGRIN VASCSLGAAH ASIVLARDYL
KVRKQFGEPL ANSQYLQFQL ADMAARLVAS RLMIRTAATA LQEEREDAIV LCSMAKLFAT
DECFAICNQA LQMHGGYGYL KDYAVQQYVR DSRVHQILEG SNEVMRMLIS RSLLQE
